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P08514

- ITA2B_HUMAN

UniProt

P08514 - ITA2B_HUMAN

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Protein
Integrin alpha-IIb
Gene
ITGA2B, GP2B, ITGAB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi274 – 2829 Reviewed prediction
Calcium bindingi328 – 3369 Reviewed prediction
Calcium bindingi396 – 4049 Reviewed prediction
Calcium bindingi457 – 4659 Reviewed prediction

GO - Molecular functioni

  1. extracellular matrix binding Source: Ensembl
  2. identical protein binding Source: IntAct
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. axon guidance Source: Reactome
  2. blood coagulation Source: Reactome
  3. cell adhesion Source: ProtInc
  4. cell-matrix adhesion Source: Ensembl
  5. extracellular matrix organization Source: Reactome
  6. integrin-mediated signaling pathway Source: UniProtKB-KW
  7. platelet activation Source: Reactome
  8. platelet aggregation Source: Ensembl
  9. platelet degranulation Source: Reactome
  10. positive regulation of leukocyte migration Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_13552. Integrin cell surface interactions.
REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_163906. ECM proteoglycans.
REACT_22272. Signal transduction by L1.
SignaLinkiP08514.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin alpha-IIb
Alternative name(s):
GPalpha IIb
Short name:
GPIIb
Platelet membrane glycoprotein IIb
CD_antigen: CD41
Cleaved into the following 3 chains:
Gene namesi
Name:ITGA2B
Synonyms:GP2B, ITGAB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:6138. ITGA2B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 993962Extracellular Reviewed prediction
Add
BLAST
Transmembranei994 – 101926Helical; Reviewed prediction
Add
BLAST
Topological domaini1020 – 103920Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. external side of plasma membrane Source: Ensembl
  3. focal adhesion Source: Ensembl
  4. integral component of plasma membrane Source: ProtInc
  5. integrin complex Source: InterPro
  6. plasma membrane Source: Reactome
  7. platelet alpha granule membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Glanzmann thrombasthenia (GT) [MIM:273800]: A common inherited disease of platelet aggregation. It is characterized by mucocutaneous bleeding of mild-to-moderate severity. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb-IIIa complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the GPIIb-IIIa complex at reduced levels, have detectable amounts of fibrinogen, and have low or moderate clot retraction capability.
Note: The disease is caused by mutations affecting the gene represented in this entry.20 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti86 – 861L → P in GT; cells co-transfected with mutated alpha-IIb and wild-type beta-3 scarcely expressed the alpha-IIb/beta-3 complex. 1 Publication
VAR_030445
Natural varianti139 – 1391A → V in GT. 1 Publication
VAR_030446
Natural varianti161 – 1611C → W in GT. 1 Publication
VAR_030447
Natural varianti174 – 1741Y → H in GT; abolishes the binding function of alpha-IIb/beta-3 for soluble ligands without disturbing alpha-IIb/beta-3 expression; functional defect is likely caused by its allosteric effect rather than by a defect in the ligand-binding site itself. 1 Publication
VAR_030448
Natural varianti176 – 1761P → A in GT; impairs surface expression of alpha-IIb/beta-3 and abrogates ligand binding to the activated integrin. 2 Publications
VAR_009885
Natural varianti176 – 1761P → L in GT; impairs surface expression of alpha-IIb/beta-3. 1 Publication
VAR_009886
Natural varianti202 – 2021F → C in GT; associated with abrogation of alpha-IIb/beta-3 complex formation. 1 Publication
VAR_030449
Natural varianti207 – 2071T → I in GT. 1 Publication
VAR_030450
Natural varianti214 – 2141L → P in GT; disrupts the structural conformation and the ligand binding properties of the heterodimeric complex; in addition the mutation appears to confer susceptibility to proteolysis. 1 Publication
VAR_030451
Natural varianti222 – 2221F → L in GT. 1 Publication
VAR_030452
Natural varianti267 – 2671G → E in GT. 1 Publication
VAR_030453
Natural varianti273 – 2731G → D in GT; alters the heterodimer conformation thus impairing their intracellular transport. 1 Publication
VAR_003979
Natural varianti320 – 3201F → S in GT; type I; impairs surface expression of alpha-IIb/beta-3. 1 Publication
VAR_009887
Natural varianti329 – 3291V → F in GT; expression of mutant subunit alpha-IIb/bet-3 is 28% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 1 Publication
VAR_030454
Natural varianti355 – 3551E → K in GT; type I; impairs surface expression of alpha-IIb/beta-3. 2 Publications
VAR_009888
Natural varianti358 – 3581R → H in GT; type II. 1 Publication
VAR_003980
Natural varianti380 – 3801G → D in GT. 1 Publication
VAR_030455
Natural varianti405 – 4051I → T in GT; expression of mutant subunit alpha-IIb/bet-3 is 11% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 3 Publications
VAR_030456
Natural varianti412 – 4121G → R in GT. 1 Publication
VAR_030457
Natural varianti449 – 4491G → D in GT; type I. 1 Publication
VAR_003981
Natural varianti456 – 4572Missing in GT; alteres the conformation of heterodimers such that they were neither recognized by the heterodimer-specific antibody A2A9 nor able to undergo further intracellular processing or transport to the cell surface.
VAR_030458
Natural varianti581 – 5811A → D in GT. 1 Publication
VAR_030459
Natural varianti596 – 5961I → T in GT; type I. 3 Publications
VAR_030460
Natural varianti705 – 7051C → R in GT; type II; the rate of subunit maturation and the surface exposure of ghlycoprotein IIb/beta-3 are strongly reduced. 3 Publications
VAR_030461
Natural varianti752 – 7521L → V in GT. 1 Publication
VAR_030462
Natural varianti755 – 7551R → P in GT. 1 Publication
VAR_030463
Natural varianti778 – 7781Q → P in GT; type II. 3 Publications
VAR_003982
Natural varianti847 – 8471L → P in GT. 1 Publication
VAR_030464
Natural varianti934 – 9341V → F in GT; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype. 1 Publication
VAR_069917
Natural varianti943 – 9431P → L in GT; marked reduction in the rate of surface expression. 1 Publication
VAR_030465
Natural varianti957 – 9571S → L in GT; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype; the mutation may interfere with correct folding of the protein. 1 Publication
VAR_069918
Natural varianti982 – 9821V → M in GT; much reduced surface expression of alpha-IIb/beta-3 and a block in the maturation of pro-alpha-IIb. 2 Publications
VAR_030466
Natural varianti1026 – 10261R → Q in GT and BDPLT16; results in low surface expression of the mutant protein. 2 Publications
VAR_030468
Bleeding disorder, platelet-type 16 (BDPLT16) [MIM:187800]: An autosomal dominant form of congenital macrothrombocytopenia associated with platelet anisocytosis. It is a disorder of platelet production. Affected individuals may have no or only mildly increased bleeding tendency. In vitro studies show mild platelet functional abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1026 – 10261R → Q in GT and BDPLT16; results in low surface expression of the mutant protein. 2 Publications
VAR_030468
Natural varianti1026 – 10261R → W in BDPLT16; results in abnormal membrane ruffling and cytoplasmic protrusions as well as defective proplatelet formation. 1 Publication
VAR_069919

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1029 – 10302PP → AA: Imparts constitutive activity (ligand-binding) to alpha-IIb/beta-3. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi187800. phenotype.
273800. phenotype.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
853. Fetal and neonatal alloimmune thrombocytopenia.
849. Glanzmann thrombasthenia.
PharmGKBiPA29938.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 31312 Publications
Add
BLAST
Chaini32 – 10391008Integrin alpha-IIb
PRO_0000016275Add
BLAST
Chaini32 – 887856Integrin alpha-IIb heavy chain
PRO_0000016276Add
BLAST
Chaini891 – 1039149Integrin alpha-IIb light chain, form 1
PRO_0000292348Add
BLAST
Chaini903 – 1039137Integrin alpha-IIb light chain, form 2
PRO_0000016277Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...)1 Publication
Disulfide bondi87 ↔ 961 Publication
Disulfide bondi138 ↔ 1611 Publication
Disulfide bondi177 ↔ 1981 Publication
Glycosylationi280 – 2801N-linked (GlcNAc...)1 Publication
Disulfide bondi504 ↔ 5151 Publication
Disulfide bondi521 ↔ 5761 Publication
Glycosylationi601 – 6011N-linked (GlcNAc...)2 Publications
Disulfide bondi633 ↔ 6391 Publication
Disulfide bondi705 ↔ 7181 Publication
Glycosylationi711 – 7111N-linked (GlcNAc...)1 Publication
Disulfide bondi857 ↔ 911Interchain (between heavy and light chains)1 Publication
Glycosylationi874 – 8741O-linked (GalNAc...); in alloantigen HPA-3B
Glycosylationi878 – 8781O-linked (GalNAc...)1 Publication
Modified residuei891 – 8911Pyrrolidone carboxylic acid; in light chain form 1
Disulfide bondi916 ↔ 9211 Publication
Glycosylationi962 – 9621N-linked (GlcNAc...)

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP08514.
PRIDEiP08514.

2D gel databases

OGPiP08514.

PTM databases

PhosphoSiteiP08514.

Miscellaneous databases

PMAP-CutDBiQ17R67.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 were identified in platelets and megakaryocytes, but not in reticulocytes or in Jurkat and U-937 white blood cell line. Isoform 3 is expressed by leukemia, prostate adenocarcinoma and melanoma cells but not by platelets or normal prostate or breast epithelial cells.

Gene expression databases

ArrayExpressiP08514.
BgeeiP08514.
CleanExiHS_ITGA2B.
GenevestigatoriP08514.

Organism-specific databases

HPAiCAB018611.
HPA031168.
HPA031169.
HPA031170.
HPA031171.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-IIb associates with beta-3. Directly interacts with RNF181. Interacts (via C-terminus cytoplasmic tail region) with CIB1; the interaction is direct and calcium-dependent. Interacts (via C-terminus cytoplasmic tail region) with CIB2, CIB3 and CIB4; the interactions are stabilized/increased in a calcium and magnesium-dependent manner.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-702693,EBI-702693
ITGB3P0510611EBI-702693,EBI-702847

Protein-protein interaction databases

BioGridi109881. 10 interactions.
DIPiDIP-68N.
IntActiP08514. 1 interaction.
STRINGi9606.ENSP00000262407.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 383
Beta strandi40 – 434
Beta strandi52 – 587
Beta strandi60 – 623
Beta strandi64 – 707
Beta strandi78 – 803
Beta strandi82 – 887
Beta strandi93 – 953
Beta strandi107 – 1104
Beta strandi113 – 1186
Beta strandi126 – 1316
Beta strandi134 – 1396
Beta strandi143 – 1486
Beta strandi151 – 1533
Beta strandi160 – 1645
Turni166 – 1683
Beta strandi171 – 1744
Helixi183 – 1886
Turni189 – 1935
Beta strandi202 – 2065
Beta strandi211 – 2166
Helixi219 – 2224
Beta strandi225 – 2306
Helixi231 – 2377
Helixi259 – 2613
Beta strandi268 – 2736
Beta strandi279 – 2813
Beta strandi283 – 2886
Helixi291 – 2944
Beta strandi297 – 3015
Beta strandi307 – 3126
Beta strandi324 – 3274
Beta strandi330 – 3334
Beta strandi336 – 3416
Beta strandi345 – 3484
Turni349 – 3513
Beta strandi352 – 3554
Beta strandi358 – 3625
Beta strandi366 – 3683
Beta strandi375 – 3795
Beta strandi391 – 3955
Beta strandi400 – 4023
Beta strandi404 – 4096
Beta strandi413 – 4175
Beta strandi419 – 4235
Beta strandi427 – 4304
Beta strandi435 – 4395
Beta strandi450 – 4567
Beta strandi458 – 4636
Beta strandi465 – 4706
Helixi471 – 4733
Beta strandi475 – 4795
Beta strandi484 – 49310
Beta strandi507 – 5093
Beta strandi512 – 52514
Beta strandi534 – 5418
Turni542 – 5443
Helixi547 – 5493
Beta strandi551 – 5544
Turni555 – 5573
Beta strandi559 – 5679
Beta strandi575 – 5839
Helixi586 – 5883
Beta strandi596 – 6038
Beta strandi616 – 6194
Beta strandi622 – 6276
Turni634 – 6374
Beta strandi643 – 6519
Beta strandi653 – 6553
Beta strandi662 – 6709
Beta strandi678 – 6836
Beta strandi688 – 6958
Beta strandi705 – 7084
Beta strandi710 – 7134
Beta strandi715 – 7217
Beta strandi728 – 73811
Beta strandi746 – 75510
Beta strandi759 – 7613
Beta strandi767 – 7748
Beta strandi779 – 79214
Beta strandi810 – 81910
Beta strandi821 – 8233
Beta strandi825 – 83612
Beta strandi842 – 85413
Beta strandi856 – 8616
Beta strandi906 – 9094
Turni911 – 9133
Beta strandi916 – 92611
Beta strandi931 – 94010
Helixi942 – 9454
Beta strandi952 – 96514
Beta strandi967 – 9693
Beta strandi977 – 98812
Turni991 – 9944
Helixi997 – 102024
Beta strandi1022 – 10243
Turni1025 – 10273
Helixi1028 – 10314
Turni1035 – 10384

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPKNMR-A1020-1039[»]
1DPQNMR-A1020-1039[»]
1JX5model-A32-483[»]
1KUPNMR-A1018-1028[»]
1KUZNMR-A1018-1028[»]
1M8ONMR-A1020-1039[»]
1RN0model-A32-482[»]
1S4WNMR-A1020-1039[»]
1TYEX-ray2.90A/C/E32-483[»]
1UV9model-A32-973[»]
2K1ANMR-A989-1029[»]
2K9JNMR-A989-1029[»]
2KNCNMR-A991-1039[»]
2VC2X-ray3.10A32-483[»]
2VDKX-ray2.80A32-483[»]
2VDLX-ray2.75A32-483[»]
2VDMX-ray2.90A32-483[»]
2VDNX-ray2.90A32-483[»]
2VDOX-ray2.51A32-483[»]
2VDPX-ray2.80A32-483[»]
2VDQX-ray2.59A32-483[»]
2VDRX-ray2.40A32-483[»]
3FCSX-ray2.55A/C32-989[»]
3FCUX-ray2.90A/C/E32-488[»]
3NIDX-ray2.30A/C32-488[»]
3NIFX-ray2.40A/C32-488[»]
3NIGX-ray2.25A/C32-488[»]
3T3MX-ray2.60A/C32-488[»]
3T3PX-ray2.20A/C32-488[»]
3ZDXX-ray2.45A/C32-488[»]
3ZDYX-ray2.45A/C32-488[»]
3ZDZX-ray2.75A/C32-488[»]
3ZE0X-ray2.95A/C32-488[»]
3ZE1X-ray3.00A/C32-488[»]
3ZE2X-ray2.35A/C32-488[»]
4CAKelectron microscopy20.50A32-989[»]
ProteinModelPortaliP08514.
SMRiP08514. Positions 32-989, 991-1039.

Miscellaneous databases

EvolutionaryTraceiP08514.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati35 – 9662FG-GAP 1
Add
BLAST
Repeati110 – 17364FG-GAP 2
Add
BLAST
Repeati186 – 23853FG-GAP 3
Add
BLAST
Repeati251 – 31060FG-GAP 4
Add
BLAST
Repeati311 – 37161FG-GAP 5
Add
BLAST
Repeati373 – 43260FG-GAP 6
Add
BLAST
Repeati434 – 49663FG-GAP 7
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1022 – 10265GFFKR motif

Sequence similaritiesi

Contains 7 FG-GAP repeats.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG26407.
HOGENOMiHOG000231603.
HOVERGENiHBG006186.
InParanoidiP08514.
KOiK06476.
OMAiCFNIQMC.
OrthoDBiEOG7TMZQZ.
PhylomeDBiP08514.
TreeFamiTF105391.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
[Graphical view]
PfamiPF01839. FG-GAP. 1 hit.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P08514-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MARALCPLQA LWLLEWVLLL LGPCAAPPAW ALNLDPVQLT FYAGPNGSQF     50
GFSLDFHKDS HGRVAIVVGA PRTLGPSQEE TGGVFLCPWR AEGGQCPSLL 100
FDLRDETRNV GSQTLQTFKA RQGLGASVVS WSDVIVACAP WQHWNVLEKT 150
EEAEKTPVGS CFLAQPESGR RAEYSPCRGN TLSRIYVEND FSWDKRYCEA 200
GFSSVVTQAG ELVLGAPGGY YFLGLLAQAP VADIFSSYRP GILLWHVSSQ 250
SLSFDSSNPE YFDGYWGYSV AVGEFDGDLN TTEYVVGAPT WSWTLGAVEI 300
LDSYYQRLHR LRGEQMASYF GHSVAVTDVN GDGRHDLLVG APLYMESRAD 350
RKLAEVGRVY LFLQPRGPHA LGAPSLLLTG TQLYGRFGSA IAPLGDLDRD 400
GYNDIAVAAP YGGPSGRGQV LVFLGQSEGL RSRPSQVLDS PFPTGSAFGF 450
SLRGAVDIDD NGYPDLIVGA YGANQVAVYR AQPVVKASVQ LLVQDSLNPA 500
VKSCVLPQTK TPVSCFNIQM CVGATGHNIP QKLSLNAELQ LDRQKPRQGR 550
RVLLLGSQQA GTTLNLDLGG KHSPICHTTM AFLRDEADFR DKLSPIVLSL 600
NVSLPPTEAG MAPAVVLHGD THVQEQTRIV LDCGEDDVCV PQLQLTASVT 650
GSPLLVGADN VLELQMDAAN EGEGAYEAEL AVHLPQGAHY MRALSNVEGF 700
ERLICNQKKE NETRVVLCEL GNPMKKNAQI GIAMLVSVGN LEEAGESVSF 750
QLQIRSKNSQ NPNSKIVLLD VPVRAEAQVE LRGNSFPASL VVAAEEGERE 800
QNSLDSWGPK VEHTYELHNN GPGTVNGLHL SIHLPGQSQP SDLLYILDIQ 850
PQGGLQCFPQ PPVNPLKVDW GLPIPSPSPI HPAHHKRDRR QIFLPEPEQP 900
SRLQDPVLVS CDSAPCTVVQ CDLQEMARGQ RAMVTVLAFL WLPSLYQRPL 950
DQFVLQSHAW FNVSSLPYAV PPLSLPRGEA QVWTQLLRAL EERAIPIWWV 1000
LVGVLGGLLL LTILVLAMWK VGFFKRNRPP LEEDDEEGE 1039
Length:1,039
Mass (Da):113,377
Last modified:April 14, 2009 - v3
Checksum:i063EE298E026F116
GO
Isoform 2 (identifier: P08514-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     948-981: Missing.

Show »
Length:1,005
Mass (Da):109,574
Checksum:i81C09F0D904CB534
GO
Isoform 3 (identifier: P08514-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     910-1039: SCDSAPCTVV...PLEEDDEEGE → VSRLSGLWPG...ATLGPWEHFK

Show »
Length:953
Mass (Da):103,218
Checksum:i0100D4C5919320BE
GO

Polymorphismi

Position 874 is associated with platelet-specific alloantigen HPA-3/BAK/LEK. HPA-3A/BAK(A)/LEK(A) has Ile-874 and HPA-3B/BAK(B)/LEK(B) has Ser-874. HPA-3B is involved in neonatal alloimmune thrombocytopenia (NAIT or NATP).

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401T → I.1 Publication
Corresponds to variant rs5915 [ dbSNP | Ensembl ].
VAR_014176
Natural varianti86 – 861L → P in GT; cells co-transfected with mutated alpha-IIb and wild-type beta-3 scarcely expressed the alpha-IIb/beta-3 complex. 1 Publication
VAR_030445
Natural varianti139 – 1391A → V in GT. 1 Publication
VAR_030446
Natural varianti161 – 1611C → W in GT. 1 Publication
VAR_030447
Natural varianti174 – 1741Y → H in GT; abolishes the binding function of alpha-IIb/beta-3 for soluble ligands without disturbing alpha-IIb/beta-3 expression; functional defect is likely caused by its allosteric effect rather than by a defect in the ligand-binding site itself. 1 Publication
VAR_030448
Natural varianti176 – 1761P → A in GT; impairs surface expression of alpha-IIb/beta-3 and abrogates ligand binding to the activated integrin. 2 Publications
VAR_009885
Natural varianti176 – 1761P → L in GT; impairs surface expression of alpha-IIb/beta-3. 1 Publication
VAR_009886
Natural varianti202 – 2021F → C in GT; associated with abrogation of alpha-IIb/beta-3 complex formation. 1 Publication
VAR_030449
Natural varianti207 – 2071T → I in GT. 1 Publication
VAR_030450
Natural varianti214 – 2141L → P in GT; disrupts the structural conformation and the ligand binding properties of the heterodimeric complex; in addition the mutation appears to confer susceptibility to proteolysis. 1 Publication
VAR_030451
Natural varianti222 – 2221F → L in GT. 1 Publication
VAR_030452
Natural varianti267 – 2671G → E in GT. 1 Publication
VAR_030453
Natural varianti273 – 2731G → D in GT; alters the heterodimer conformation thus impairing their intracellular transport. 1 Publication
VAR_003979
Natural varianti313 – 3131G → A.2 Publications
Corresponds to variant rs1126554 [ dbSNP | Ensembl ].
VAR_054820
Natural varianti320 – 3201F → S in GT; type I; impairs surface expression of alpha-IIb/beta-3. 1 Publication
VAR_009887
Natural varianti329 – 3291V → F in GT; expression of mutant subunit alpha-IIb/bet-3 is 28% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 1 Publication
VAR_030454
Natural varianti355 – 3551E → K in GT; type I; impairs surface expression of alpha-IIb/beta-3. 2 Publications
VAR_009888
Natural varianti358 – 3581R → H in GT; type II. 1 Publication
VAR_003980
Natural varianti380 – 3801G → D in GT. 1 Publication
VAR_030455
Natural varianti405 – 4051I → T in GT; expression of mutant subunit alpha-IIb/bet-3 is 11% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum. 3 Publications
VAR_030456
Natural varianti412 – 4121G → R in GT. 1 Publication
VAR_030457
Natural varianti449 – 4491G → D in GT; type I. 1 Publication
VAR_003981
Natural varianti456 – 4572Missing in GT; alteres the conformation of heterodimers such that they were neither recognized by the heterodimer-specific antibody A2A9 nor able to undergo further intracellular processing or transport to the cell surface.
VAR_030458
Natural varianti581 – 5811A → D in GT. 1 Publication
VAR_030459
Natural varianti596 – 5961I → T in GT; type I. 3 Publications
VAR_030460
Natural varianti649 – 6491V → L.
Corresponds to variant rs7207402 [ dbSNP | Ensembl ].
VAR_054821
Natural varianti705 – 7051C → R in GT; type II; the rate of subunit maturation and the surface exposure of ghlycoprotein IIb/beta-3 are strongly reduced. 3 Publications
VAR_030461
Natural varianti752 – 7521L → V in GT. 1 Publication
VAR_030462
Natural varianti755 – 7551R → P in GT. 1 Publication
VAR_030463
Natural varianti778 – 7781Q → P in GT; type II. 3 Publications
VAR_003982
Natural varianti847 – 8471L → P in GT. 1 Publication
VAR_030464
Natural varianti874 – 8741I → S Alloantigen HPA-3B. 1 Publication
Corresponds to variant rs5911 [ dbSNP | Ensembl ].
VAR_003983
Natural varianti934 – 9341V → F in GT; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype. 1 Publication
VAR_069917
Natural varianti943 – 9431P → L in GT; marked reduction in the rate of surface expression. 1 Publication
VAR_030465
Natural varianti957 – 9571S → L in GT; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype; the mutation may interfere with correct folding of the protein. 1 Publication
VAR_069918
Natural varianti968 – 9681Y → N.1 Publication
Corresponds to variant rs5914 [ dbSNP | Ensembl ].
VAR_014177
Natural varianti982 – 9821V → M in GT; much reduced surface expression of alpha-IIb/beta-3 and a block in the maturation of pro-alpha-IIb. 2 Publications
VAR_030466
Natural varianti989 – 9891A → T.2 Publications
Corresponds to variant rs78165611 [ dbSNP | Ensembl ].
VAR_030467
Natural varianti1026 – 10261R → Q in GT and BDPLT16; results in low surface expression of the mutant protein. 2 Publications
VAR_030468
Natural varianti1026 – 10261R → W in BDPLT16; results in abnormal membrane ruffling and cytoplasmic protrusions as well as defective proplatelet formation. 1 Publication
VAR_069919

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei910 – 1039130SCDSA…DEEGE → VSRLSGLWPGLPGTHGAEGM GGGRGVRVCCGPLWATLGPW EHFK in isoform 3.
VSP_002736Add
BLAST
Alternative sequencei948 – 98134Missing in isoform 2.
VSP_002737Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231P → A in AAA35926. 1 Publication
Sequence conflicti120 – 1201A → S in BAG37735. 1 Publication
Sequence conflicti287 – 2882GA → VP in AAA53150. 1 Publication
Sequence conflicti346 – 3461E → D in AAA35926. 1 Publication
Sequence conflicti565 – 5651N → D in AAA35926. 1 Publication
Sequence conflicti566 – 5661L → V in CAA29987. 1 Publication
Sequence conflicti633 – 6331C → S in AAA60114. 1 Publication
Sequence conflicti729 – 7291Q → E in CAA29987. 1 Publication
Sequence conflicti971 – 9711P → A in AAA53150. 1 Publication
Sequence conflicti1029 – 10291P → H in AAA35926. 1 Publication
Sequence conflicti1029 – 10291P → H in AAA52588. 1 Publication
Sequence conflicti1030 – 10301P → T in AAA52588. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02764 mRNA. Translation: AAA60114.1.
M34480 mRNA. Translation: AAA35926.1.
M34344, M33319, M33320 Genomic DNA. Translation: AAA53150.1.
M54799 Genomic DNA. Translation: AAA52599.1.
X06831 mRNA. Translation: CAA29987.1.
M18085 mRNA. Translation: AAA52597.1.
M22568 Genomic DNA. Translation: AAA52587.1.
M22569 Genomic DNA. Translation: AAA52588.1.
AF098114 mRNA. Translation: AAC98507.1.
AK315335 mRNA. Translation: BAG37735.1.
AC003043 Genomic DNA. No translation available.
BC117443 mRNA. Translation: AAI17444.1.
BC126442 mRNA. Translation: AAI26443.1.
CCDSiCCDS32665.1. [P08514-1]
PIRiA34269.
RefSeqiNP_000410.2. NM_000419.3. [P08514-1]
UniGeneiHs.411312.

Genome annotation databases

EnsembliENST00000262407; ENSP00000262407; ENSG00000005961. [P08514-1]
ENST00000353281; ENSP00000340536; ENSG00000005961. [P08514-2]
GeneIDi3674.
KEGGihsa:3674.
UCSCiuc002igt.1. human. [P08514-1]

Polymorphism databases

DMDMi226694183.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02764 mRNA. Translation: AAA60114.1 .
M34480 mRNA. Translation: AAA35926.1 .
M34344 , M33319 , M33320 Genomic DNA. Translation: AAA53150.1 .
M54799 Genomic DNA. Translation: AAA52599.1 .
X06831 mRNA. Translation: CAA29987.1 .
M18085 mRNA. Translation: AAA52597.1 .
M22568 Genomic DNA. Translation: AAA52587.1 .
M22569 Genomic DNA. Translation: AAA52588.1 .
AF098114 mRNA. Translation: AAC98507.1 .
AK315335 mRNA. Translation: BAG37735.1 .
AC003043 Genomic DNA. No translation available.
BC117443 mRNA. Translation: AAI17444.1 .
BC126442 mRNA. Translation: AAI26443.1 .
CCDSi CCDS32665.1. [P08514-1 ]
PIRi A34269.
RefSeqi NP_000410.2. NM_000419.3. [P08514-1 ]
UniGenei Hs.411312.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DPK NMR - A 1020-1039 [» ]
1DPQ NMR - A 1020-1039 [» ]
1JX5 model - A 32-483 [» ]
1KUP NMR - A 1018-1028 [» ]
1KUZ NMR - A 1018-1028 [» ]
1M8O NMR - A 1020-1039 [» ]
1RN0 model - A 32-482 [» ]
1S4W NMR - A 1020-1039 [» ]
1TYE X-ray 2.90 A/C/E 32-483 [» ]
1UV9 model - A 32-973 [» ]
2K1A NMR - A 989-1029 [» ]
2K9J NMR - A 989-1029 [» ]
2KNC NMR - A 991-1039 [» ]
2VC2 X-ray 3.10 A 32-483 [» ]
2VDK X-ray 2.80 A 32-483 [» ]
2VDL X-ray 2.75 A 32-483 [» ]
2VDM X-ray 2.90 A 32-483 [» ]
2VDN X-ray 2.90 A 32-483 [» ]
2VDO X-ray 2.51 A 32-483 [» ]
2VDP X-ray 2.80 A 32-483 [» ]
2VDQ X-ray 2.59 A 32-483 [» ]
2VDR X-ray 2.40 A 32-483 [» ]
3FCS X-ray 2.55 A/C 32-989 [» ]
3FCU X-ray 2.90 A/C/E 32-488 [» ]
3NID X-ray 2.30 A/C 32-488 [» ]
3NIF X-ray 2.40 A/C 32-488 [» ]
3NIG X-ray 2.25 A/C 32-488 [» ]
3T3M X-ray 2.60 A/C 32-488 [» ]
3T3P X-ray 2.20 A/C 32-488 [» ]
3ZDX X-ray 2.45 A/C 32-488 [» ]
3ZDY X-ray 2.45 A/C 32-488 [» ]
3ZDZ X-ray 2.75 A/C 32-488 [» ]
3ZE0 X-ray 2.95 A/C 32-488 [» ]
3ZE1 X-ray 3.00 A/C 32-488 [» ]
3ZE2 X-ray 2.35 A/C 32-488 [» ]
4CAK electron microscopy 20.50 A 32-989 [» ]
ProteinModelPortali P08514.
SMRi P08514. Positions 32-989, 991-1039.
ModBasei Search...

Protein-protein interaction databases

BioGridi 109881. 10 interactions.
DIPi DIP-68N.
IntActi P08514. 1 interaction.
STRINGi 9606.ENSP00000262407.

Chemistry

BindingDBi P08514.
ChEMBLi CHEMBL2111443.
DrugBanki DB00775. Tirofiban.

PTM databases

PhosphoSitei P08514.

Polymorphism databases

DMDMi 226694183.

2D gel databases

OGPi P08514.

Proteomic databases

PaxDbi P08514.
PRIDEi P08514.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262407 ; ENSP00000262407 ; ENSG00000005961 . [P08514-1 ]
ENST00000353281 ; ENSP00000340536 ; ENSG00000005961 . [P08514-2 ]
GeneIDi 3674.
KEGGi hsa:3674.
UCSCi uc002igt.1. human. [P08514-1 ]

Organism-specific databases

CTDi 3674.
GeneCardsi GC17M042460.
HGNCi HGNC:6138. ITGA2B.
HPAi CAB018611.
HPA031168.
HPA031169.
HPA031170.
HPA031171.
MIMi 187800. phenotype.
273800. phenotype.
607759. gene.
neXtProti NX_P08514.
Orphaneti 140957. Autosomal dominant macrothrombocytopenia.
853. Fetal and neonatal alloimmune thrombocytopenia.
849. Glanzmann thrombasthenia.
PharmGKBi PA29938.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG26407.
HOGENOMi HOG000231603.
HOVERGENi HBG006186.
InParanoidi P08514.
KOi K06476.
OMAi CFNIQMC.
OrthoDBi EOG7TMZQZ.
PhylomeDBi P08514.
TreeFami TF105391.

Enzyme and pathway databases

Reactomei REACT_13552. Integrin cell surface interactions.
REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_163906. ECM proteoglycans.
REACT_22272. Signal transduction by L1.
SignaLinki P08514.

Miscellaneous databases

EvolutionaryTracei P08514.
GeneWikii ITGA2B.
GenomeRNAii 3674.
NextBioi 14381.
PMAP-CutDBi Q17R67.
PROi P08514.
SOURCEi Search...

Gene expression databases

ArrayExpressi P08514.
Bgeei P08514.
CleanExi HS_ITGA2B.
Genevestigatori P08514.

Family and domain databases

InterProi IPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
[Graphical view ]
Pfami PF01839. FG-GAP. 1 hit.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view ]
PRINTSi PR01185. INTEGRINA.
SMARTi SM00191. Int_alpha. 5 hits.
[Graphical view ]
PROSITEi PS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the platelet membrane glycoprotein IIb. Homology to the alpha subunits of the vitronectin and fibronectin membrane receptors."
    Poncz M., Eisman R., Heidenreich R., Silver S.M., Vilaire G., Surrey S., Schwartz E., Bennett J.S.
    J. Biol. Chem. 262:8476-8482(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-313.
  2. "GPIIb and GPIIIa amino acid sequences deduced from human megakaryocyte cDNAs."
    Frachet P., Uzan G., Thevenon D., Denarier E., Prandini M.H., Marguerie G.
    Mol. Biol. Rep. 14:27-33(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-313.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Spleen.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  7. "Human platelets and megakaryocytes contain alternately spliced glycoprotein IIb mRNAs."
    Bray P.F., Leung C.S.-I., Shuman M.A.
    J. Biol. Chem. 265:9587-9590(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
    Tissue: Erythroleukemia.
  8. "cDNA clones for human platelet GPIIb corresponding to mRNA from megakaryocytes and HEL cells. Evidence for an extensive homology to other Arg-Gly-Asp adhesion receptors."
    Uzan G., Frachet P., Lajmanovich A., Prandini M.-H., Denarier E., Duperray A., Loftus J., Ginsberg M., Plow E., Marguerie G.
    Eur. J. Biochem. 171:87-93(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 392-1039 (ISOFORM 1).
  9. "Platelet glycoprotein IIb. Chromosomal localization and tissue expression."
    Bray P.F., Rosa J.P., Johnston G.I., Shiu D.T., Cook R.G., Lau C., Kan Y.W., McEver R.P., Shuman M.A.
    J. Clin. Invest. 80:1812-1817(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 868-1039 (ISOFORM 1).
  10. "Isolation of the human platelet glycoprotein IIb gene and characterization of the 5' flanking region."
    Prandini M.H., Denarier E., Frachet P., Uzan G., Marguerie G.
    Biochem. Biophys. Res. Commun. 156:595-601(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62 AND 1021-1039.
  11. "Platelet glycoproteins IIb and IIIa: evidence for a family of immunologically and structurally related glycoproteins in mammalian cells."
    Charo I.F., Fitzgerald L.A., Steiner B., Rall S.C., Bekeart L.S., Phillips D.R.
    Proc. Natl. Acad. Sci. U.S.A. 83:8351-8355(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 32-56 AND 903-917.
  12. "Separation of important new platelet glycoproteins (GPIa, GPIc, GPIc*, GPIIa and GMP-140) by F.P.L.C. Characterization by monoclonal antibodies and gas-phase sequencing."
    Catimel B., Parmentier S., Leung L.L., McGregor J.L.
    Biochem. J. 279:419-425(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 32-42.
  13. "Thermal stability of individual domains in platelet glycoprotein IIbIIIa."
    Makogonenko E.M., Yakubenko V.P., Ingham K.C., Medved L.V.
    Eur. J. Biochem. 237:205-211(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 32 AND 872.
  14. "Purification and partial amino acid sequence of human platelet membrane glycoproteins IIb and IIIa."
    Hiraiwa A., Matsukage A., Shiku H., Takahashi T., Naito K., Yamada K.
    Blood 69:560-564(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 487-501 AND 1026-1038.
  15. "Interchain and intrachain disulphide bonds in human platelet glycoprotein IIb. Localization of the epitopes for several monoclonal antibodies."
    Calvete J.J., Alvarez M.V., Rivas G., Hew C.L., Henschen A., Gonzalez-Rodriguez J.
    Biochem. J. 261:551-560(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 903-922 AND 934-939.
  16. "Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the alpha-subunit of human platelet glycoprotein IIb."
    Calvete J.J., Henschen A., Gonzalez-Rodriguez J.
    Biochem. J. 261:561-568(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-46; ASN-280; ASN-601 AND ASN-711.
  17. "Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression."
    Calvete J.J., Muniz-Diaz E.
    FEBS Lett. 328:30-34(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT SER-878.
  18. "Identification of a novel truncated alphaIIb integrin."
    Trikha M., Cai Y., Grignon D., Honn K.V.
    Cancer Res. 58:4771-4775(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  19. "Characterization of the beta-chain N-terminus heterogeneity and the alpha-chain C-terminus of human platelet GPIIb. Posttranslational cleavage sites."
    Calvete J.J., Schafer W., Henschen A., Gonzalez-Rodriguez J.
    FEBS Lett. 272:37-40(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC CLEAVAGE, PYROGLUTAMATE FORMATION AT GLN-891.
  20. "Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain."
    Naik U.P., Patel P.M., Parise L.V.
    J. Biol. Chem. 272:4651-4654(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIB1.
    Tissue: Fetal liver.
  21. "Calcium-dependent properties of CIB binding to the integrin alphaIIb cytoplasmic domain and translocation to the platelet cytoskeleton."
    Shock D.D., Naik U.P., Brittain J.E., Alahari S.K., Sondek J., Parise L.V.
    Biochem. J. 342:729-735(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIB1.
  22. "Bidirectional transmembrane modulation of integrin alphaIIbbeta3 conformations."
    Leisner T.M., Wencel-Drake J.D., Wang W., Lam S.C.
    J. Biol. Chem. 274:12945-12949(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 1029-PRO-PRO-1030.
  23. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-601.
    Tissue: Plasma.
  24. "RN181, a novel ubiquitin E3 ligase that interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3."
    Brophy T.M., Raab M., Daxecker H., Culligan K.G., Lehmann I., Chubb A.J., Treumann A., Moran N.
    Biochem. Biophys. Res. Commun. 369:1088-1093(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF181.
  25. "Solution structures of Ca2+-CIB1 and Mg2+-CIB1 and their interactions with the platelet integrin alphaIIb cytoplasmic domain."
    Huang H., Ishida H., Yamniuk A.P., Vogel H.J.
    J. Biol. Chem. 286:17181-17192(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIB1.
  26. "Biophysical and structural studies of the human calcium- and integrin-binding protein family: understanding their functional similarities and differences."
    Huang H., Bogstie J.N., Vogel H.J.
    Biochem. Cell Biol. 90:646-656(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIB1; CIB2; CIB3 AND CIB4.
  27. "Structural basis for the activation of platelet integrin alphaIIbbeta3 by calcium- and integrin-binding protein 1."
    Huang H., Vogel H.J.
    J. Am. Chem. Soc. 134:3864-3872(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIB1.
  28. "Inherited diseases of platelet glycoproteins: considerations for rapid molecular characterization."
    Bray P.F.
    Thromb. Haemost. 72:492-502(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON GT VARIANTS.
  29. "Polymorphism of human platelet membrane glycoprotein IIb associated with the Baka/Bakb alloantigen system."
    Lyman S., Aster R.H., Visentin G.P., Newman P.J.
    Blood 75:2343-2348(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HPA-3 (BAK).
  30. "Glanzmann thrombasthenia secondary to a Gly273-->Asp mutation adjacent to the first calcium-binding domain of platelet glycoprotein IIb."
    Poncz M., Rifat S., Coller B.S., Newman P.J., Shattil S.J., Parrella T., Fortina P., Bennett J.S.
    J. Clin. Invest. 93:172-179(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GT ASP-273.
  31. "A single amino acid substitution flanking the fourth calcium binding domain of alpha IIb prevents maturation of the alpha IIb beta 3 integrin complex."
    Wilcox D.A., Wautier J.-L., Pidard D., Newman P.J.
    J. Biol. Chem. 269:4450-4457(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GT ASP-449.
  32. "Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb. Role of the GPIIb amino terminus in integrin subunit association."
    Wilcox D.A., Paddock C.M., Lyman S., Gill J.C., Newman P.J.
    J. Clin. Invest. 95:1553-1560(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GT HIS-358.
  33. "Glanzmann thrombasthenia due to a two amino acid deletion in the fourth calcium-binding domain of alpha IIb: demonstration of the importance of calcium-binding domains in the conformation of alpha IIb beta 3."
    Basani R.B., Vilaire G., Shattil S.J., Kolodziej M.A., Bennett J.S., Poncz M.
    Blood 88:167-173(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GT VAL-456-457-ASP DEL, CHARACTERIZATION OF VARIANT GT VAL-456-457-ASP DEL.
  34. "Hematologically important mutations: Glanzmann thrombasthenia."
    French D.L., Coller B.S.
    Blood Cells Mol. Dis. 23:39-51(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GT ILE-207; THR-596 AND GLN-1026.
  35. "Glycoprotein IIb Leu214Pro mutation produces Glanzmann thrombasthenia with both quantitative and qualitative abnormalities in GPIIb/IIIa."
    Grimaldi C.M., Chen F., Wu C., Weiss H.J., Coller B.S., French D.L.
    Blood 91:1562-1571(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GT PRO-214, CHARACTERIZATION OF VARIANT GT PRO-214.
  36. "A Gln747-->Pro substitution in the IIb subunit is responsible for a moderate IIbbeta3 deficiency in Glanzmann thrombasthenia."
    Tadokoro S., Tomiyama Y., Honda S., Arai M., Yamamoto N., Shiraga M., Kosugi S., Kanakura Y., Kurata Y., Matsuzawa Y.
    Blood 92:2750-2758(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GT PRO-778.
  37. "R to Q amino acid substitution in the GFFKR sequence of the cytoplasmic domain of the integrin IIb subunit in a patient with a Glanzmann's thrombasthenia-like syndrome."
    Peyruchaud O., Nurden A.T., Milet S., Macchi L., Pannochia A., Bray P.F., Kieffer N., Bourre F.
    Blood 92:4178-4187(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BDPLT16 GLN-1026, CHARACTERIZATION OF VARIANT BDPLT16 GLN-1026.
  38. "Novel point mutations in the alphaIIb subunit (Phe289-->Ser, Glu324-->Lys and Gln747-->Pro) causing thrombasthenic phenotypes in four Japanese patients."
    Ambo H., Kamata T., Handa M., Kawai Y., Oda A., Murata M., Takada Y., Ikeda Y.
    Br. J. Haematol. 102:829-840(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GT SER-320; LYS-355 AND PRO-778.
  39. "Double heterozygosity of the GPIIb gene in a Swiss patient with Glanzmann's thrombasthenia."
    Ruan J., Peyruchaud O., Alberio L., Valles G., Clemetson K., Bourre F., Nurden A.T.
    Br. J. Haematol. 102:918-925(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GT LYS-355 AND THR-596.
  40. Cited for: VARIANTS ILE-40; SER-874 AND ASN-968.
  41. "Molecular genetic analysis of a compound heterozygote for the glycoprotein (GP) IIb gene associated with Glanzmann's thrombasthenia: disruption of the 674-687 disulfide bridge in GPIIb prevents surface exposure of GPIIb-IIIa complexes."
    Gonzalez-Manchon C., Fernandez-Pinel M., Arias-Salgado E.G., Ferrer M., Alvarez M.-V., Garcia-Munoz S., Ayuso M.S., Parrilla R.
    Blood 93:866-875(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GT ARG-705, CHARACTERIZATION OF VARIANT GT ARG-705.
  42. "A naturally occurring mutation near the amino terminus of alphaIIb defines a new region involved in ligand binding to alphaIIbbeta3."
    Basani R.B., French D.L., Vilaire G., Brown D.L., Chen F., Coller B.S., Derrick J.M., Gartner T.K., Bennett J.S., Poncz M.
    Blood 95:180-188(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GT ALA-176 AND LEU-176.
  43. "Description of 10 new mutations in platelet glycoprotein IIb (alphaIIb) and glycoprotein IIIa (beta3) genes."
    Vinciguerra C., Bordet J.C., Beaune G., Grenier C., Dechavanne M., Negrier C.
    Platelets 12:486-495(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GT TRP-161; LEU-222; ARG-412 AND PRO-847.
  44. "A Leu55 to Pro substitution in the integrin alphaIIb is responsible for a case of Glanzmann's thrombasthenia."
    Tanaka S., Hayashi T., Hori Y., Terada C., Han K.S., Ahn H.S., Bourre F., Tani Y.
    Br. J. Haematol. 118:833-835(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GT PRO-86, CHARACTERIZATION OF VARIANT GT PRO-86.
  45. "Glanzmann's thrombasthenia: identification of 19 new mutations in 30 patients."
    D'Andrea G., Colaizzo D., Vecchione G., Grandone E., Di Minno G., Margaglione M.
    Thromb. Haemost. 87:1034-1042(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GT VAL-139; ALA-176; GLU-267; ASP-380; THR-405; ASP-581; ARG-705; VAL-752 AND PRO-755.
  46. "Two novel mutations in the alpha IIb calcium-binding domains identify hydrophobic regions essential for alpha IIbbeta 3 biogenesis."
    Mitchell W.B., Li J.H., Singh F., Michelson A.D., Bussel J., Coller B.S., French D.L.
    Blood 101:2268-2276(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GT PHE-329 AND THR-405, CHARACTERIZATION OF VARIANTS GT PHE-329 AND THR-405.
  47. "A naturally occurring Tyr143His alpha IIb mutation abolishes alpha IIb beta 3 function for soluble ligands but retains its ability for mediating cell adhesion and clot retraction: comparison with other mutations causing ligand-binding defects."
    Kiyoi T., Tomiyama Y., Honda S., Tadokoro S., Arai M., Kashiwagi H., Kosugi S., Kato H., Kurata Y., Matsuzawa Y.
    Blood 101:3485-3491(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GT HIS-174, CHARACTERIZATION OF VARIANT GT HIS-174.
  48. "Triple heterozygosity in the integrin alphaIIb subunit in a patient with Glanzmann's thrombasthenia."
    Nurden A.T., Breillat C., Jacquelin B., Combrie R., Freedman J., Blanchette V.S., Schmugge M., Rand M.L.
    J. Thromb. Haemost. 2:813-819(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GT MET-982, CHARACTERIZATION OF VARIANT GT MET-982, VARIANT THR-989.
  49. "A novel Phe171Cys mutation in integrin alpha causes Glanzmann thrombasthenia by abrogating alphaIIbbeta3 complex formation."
    Rosenberg N., Landau M., Luboshitz J., Rechavi G., Seligsohn U.
    J. Thromb. Haemost. 2:1167-1175(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GT CYS-202, CHARACTERIZATION OF VARIANT GT CYS-202.
  50. "Type II Glanzmann thrombasthenia in a compound heterozygote for the alpha IIb gene. A novel missense mutation in exon 27."
    Jayo A., Pabon D., Lastres P., Jimenez-Yuste V., Gonzalez-Manchon C.
    Haematologica 91:1352-1359(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GT LEU-943, CHARACTERIZATION OF VARIANT GT LEU-943.
  51. "AlphaIIbbeta3 integrin: new allelic variants in Glanzmann thrombasthenia, effects on ITGA2B and ITGB3 mRNA splicing, expression, and structure-function."
    Jallu V., Dusseaux M., Panzer S., Torchet M.F., Hezard N., Goudemand J., de Brevern A.G., Kaplan C.
    Hum. Mutat. 31:237-246(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GT THR-405; THR-596; ARG-705; PRO-778; PHE-934; LEU-957; MET-982 AND THR-989, CHARACTERIZATION OF VARIANTS GT PHE-934 AND LEU-957.
  52. "Heterozygous ITGA2B R995W mutation inducing constitutive activation of the alphaIIbbeta3 receptor affects proplatelet formation and causes congenital macrothrombocytopenia."
    Kunishima S., Kashiwagi H., Otsu M., Takayama N., Eto K., Onodera M., Miyajima Y., Takamatsu Y., Suzumiya J., Matsubara K., Tomiyama Y., Saito H.
    Blood 117:5479-5484(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BDPLT16 TRP-1026, CHARACTERIZATION OF VARIANT BDPLT16 TRP-1026.

Entry informationi

Entry nameiITA2B_HUMAN
AccessioniPrimary (citable) accession number: P08514
Secondary accession number(s): B2RCY8
, O95366, Q14443, Q17R67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 14, 2009
Last modified: September 3, 2014
This is version 189 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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